2o94

X-ray diffraction
3Å resolution

The 97H/F mutant Structure of a glutamine-rich domain from histone deacetylase 4

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone deacetylase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 112 amino acids
Theoretical weight: 13.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56524 (Residues: 62-153; Coverage: 9%)
  • Best match: P56524-2 (Residues: 1-36)
Gene names: HDAC4, KIAA0288
Sequence domains: Glutamine rich N terminal domain of histone deacetylase 4
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2
Unit cell:
a: 189.885Å b: 61.023Å c: 60.777Å
α: 90° β: 108.61° γ: 90°
R-values:
R R work R free
0.324 0.305 0.327
Expression system: Escherichia coli